Tat-Mediated p66shc Transduction Decreased Phosphorylation of Endothelial Nitric Oxide Synthase in Endothelial Cells
The Korean Journal of Physiology and Pharmacology
;
: 199-204, 2012.
Artículo
en Inglés
| WPRIM
| ID: wpr-728100
ABSTRACT
We evaluated the role of Tat-mediated p66shc transduction on the activation of endothelial nitric oxide synthase in cultured mouse endothelial cells. To construct the Tat-p66shc fusion protein, human full length p66shc cDNA was fused with the Tat-protein transduction domain. Transduction of TAT-p66shc showed a concentration- and time-dependent manner in endothelial cells. Tat-mediated p66shc transduction showed increased hydrogen peroxide and superoxide production, compared with Tat-p66shc (S/A), serine 36 residue mutant of p66shc. Tat-mediated p66shc transduction decreased endothelial nitric oxide synthase phosphorylation in endothelial cells. Furthermore, Tat-mediated p66shc transduction augmented TNF-alpha-induced p38 MAPK phosphorylation in endothelial cells. These results suggest that Tat-mediated p66shc transduction efficiently inhibited endothelial nitric oxide synthase phosphorylation in endothelial cells.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Fosforilación
/
Serina
/
ADN Complementario
/
Superóxidos
/
Células Endoteliales
/
Proteínas Quinasas p38 Activadas por Mitógenos
/
Óxido Nítrico Sintasa de Tipo III
/
Peróxido de Hidrógeno
Límite:
Animales
/
Humanos
Idioma:
Inglés
Revista:
The Korean Journal of Physiology and Pharmacology
Año:
2012
Tipo del documento:
Artículo
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